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Sequence variation in the outer membrane protein-encoding gene cmeC, conferring multidrug resistance among Campylobacter jejuni and Campylobacter coli strains isolated from different hosts.

ABSTRACT: A novel PCR primer pair was used to detect the presence of cmeC in 131 Campylobacter jejuni and C. coli strains isolated from various hosts (cattle, turkeys, humans, and pigs). DNA sequence analysis revealed a high degree of genetic variation between the two species, while extremely limited genetic variation among isolates of the same species was detected.

SUBMITTER: Fakhr MK

PROVIDER: S-EPMC2045336 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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Sequence variation in the outer membrane protein-encoding gene cmeC, conferring multidrug resistance among Campylobacter jejuni and Campylobacter coli strains isolated from different hosts.

Fakhr Mohamed K MK Logue Catherine M CM

Journal of clinical microbiology 20070725 10

A novel PCR primer pair was used to detect the presence of cmeC in 131 Campylobacter jejuni and C. coli strains isolated from various hosts (cattle, turkeys, humans, and pigs). DNA sequence analysis revealed a high degree of genetic variation between the two species, while extremely limited genetic variation among isolates of the same species was detected. ...[more]

PMID: 17652470

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Project description:Campylobacter jejuni is the leading bacterial cause of human enteritis in many industrialized countries. There is no commercial vaccine against C. jejuni available to date. CmeC is an essential outer membrane component of CmeABC multidrug efflux pump that plays a critical role in antibiotic resistance and in vivo colonization of C. jejuni. CmeC is prevalent in C. jejuni strains and is dramatically induced and immunogenic in vivo. In this study, we analyzed CmeC sequence homology, examined in vitro immune protection of CmeC peptide antibodies, and produced full-length recombinant CmeC (rCmeC) for evaluating immunogenicity and protective efficacy of the CmeC subunit vaccine against C. jejuni using chicken model system. Amino acid sequences of CmeC from 24 diverse C. jejuni strains were determined and subjected to alignment, which revealed that CmeC is highly conserved in C. jejuni with a identity ranging from 97.3% to 100%. CmeC peptide antibodies inhibited the function of CmeABC efflux pump and enhanced susceptibility of C. jejuni to bile salts, the natural antimicrobial present in the intestine. Two full-length rCmeC proteins with N- or C-terminal His tag were produced in E. coli; the N-terminal His-tagged rCmeC with high purity and yield was obtained by single step affinity purification. The purified rCmeC was used in two vaccination trials using a chicken model of C. jejuni infection. Stimulation of CmeC-specific serum IgG responses via oral vaccination required immunization with higher doses of rCmeC (200μg) together with 70μg of mucosal adjuvant mLT (modified E. coli heat-labile enterotoxin). Subcutaneous vaccination of chickens with rCmeC remarkably stimulated both serum IgG and IgA responses. However, CmeC-specific intestinal secretory IgA response was not significantly stimulated regardless of vaccination regimen and the rCmeC vaccination did not confer protection against C. jejuni infection. Together, these findings provide further compelling evidence that CmeC is a promising subunit vaccine candidate against C. jejuni infection. However, the CmeC vaccination regimen should be optimized to enhance CmeC-specific mucosal immune response in for protection against C. jejuni.

Dataset Information

Sequence variation in the outer membrane protein-encoding gene cmeC, conferring multidrug resistance among Campylobacter jejuni and Campylobacter coli strains isolated from different hosts.

Publications

Sequence variation in the outer membrane protein-encoding gene cmeC, conferring multidrug resistance among Campylobacter jejuni and Campylobacter coli strains isolated from different hosts.

Similar Datasets

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